publication . Article . 2003

Thermodynamic Effects of Replacements of Pro Residues in Helix Interiors of Maltose-Binding Protein

Prajapati, RS; Lingaraju, GM; Bacchawat, Kiran; Surolia, Avadhesha; Varadarajan, Raghavan;
Open Access
  • Published: 01 Jan 2003
  • Publisher: Wiley-Liss, Inc.
  • Country: India
Abstract
Introduction of Pro residues into helix interiors results in protein destabilization. It is currently unclear if the converse substitution (i.e., replacement of Pro residues that naturally occur in helix interiors would be stabilizing). Maltose-binding protein is a large 370-amino acid protein that contains 21 Pro residues. Of these, three nonconserved residues (P48, P133, and P159) occur at helix interiors. Each of the residues was replaced with Ala and Ser. Stabilities were characterized by differential scanning calorimetry (DSC) as a function of pH and by isothermal urea denaturation studies as a function of temperature. The P48S and P48A mutants were found t...
Subjects
free text keywords: Molecular Biophysics Unit
25 references, page 1 of 2

1. Sauer UH, San DP, Matthews BW. Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions. J Biol Chem 1992;267:2393-2399.

2. Gray TM, Arnoys EJ, Blankespoor S, Born T, Jagar R, Everman R, Plowman D, Stair A, Zhang D. Destabilizing effect of proline substitutions in two helical regions of T4 lysozyme: leucine 66 to proline and leucine 91 to proline. Protein Sci 1996;5:742-751.

3. Gunasekaran K, Nagarajaram HA, Ramakrishnan C, Balaram P. Stereochemical punctuation marks in protein structures: glycine and proline containing helix stop signals. J Mol Biol 1998;275:917-932. [OpenAIRE]

4. Ganesh C, Shah AN, Swaminathan CP, Surolia A, Varadarajan R. Thermodynamic characterization of the reversible, two-state unfolding of maltose binding protein, a large two-domain protein. Biochemistry 1997;36:5020 -5028.

5. Sheshadri S, Lingaraju GM, Varadarajan R. Denaturant mediated unfolding of both native and molten globule states of maltose binding protein are accompanied by large deltaCp's. Protein Sci 1999;8:1689 -1695. [OpenAIRE]

6. Spurlino JC, Lu GY, Quiocho FA. The 2.3-A resolution structure of the maltose-or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. J Biol Chem 1991;266: 5202-5219.

7. Sharff AJ, Rodseth LE, Spurlino JC, Quiocho FA. Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis. Biochemistry 1992;31: 10657-10663.

8. Chakrabarti A, Srivastava S, Swaminathan CP, Surolia A, Varadarajan R. Thermodynamics of replacing an alpha-helical Pro residue in the P40S mutant of Escherichia coli thioredoxin. Protein Sci 1999;8:2455-2459. [OpenAIRE]

9. Duplay P, Bedouelle H, Fowler A, Zabin I, Saurin W, Hofnung M. Sequences of the malE gene and of its product, the maltosebinding protein of Escherichia coli K12. J Biol Chem 1984;259: 10606 -10613.

10. Martineau P, Szmelcman S, Spurlino JC, Quiocho FA, Hofnung M. Genetic approach to the role of tryptophan residues in the activities and fluorescence of a bacterial periplasmic maltosebinding protein. J Mol Biol 1990;214:337-352. [OpenAIRE]

11. Ganesh C, Banerjee A, Shah A, Varadarajan R. Disordered N-terminal residues affect the folding thermodynamics and kinetics of maltose binding protein. FEBS Lett 1999;454:307-311.

12. Schellman JA. The thermodynamic stability of proteins. Annu Rev Biophys Biophys Chem 1987;16:115-137. [OpenAIRE]

13. Chen BL, Schellman JA. Low-temperature unfolding of a mutant of phage T4 lysozyme. I. Equilibrium studies. Biochemistry 1989; 28:685- 691. [OpenAIRE]

14. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE. The Protein Data Bank. Nucleic Acids Res 2000;28:235-242.

15. McDonald IK, Thornton JM. Satisfying hydrogen bonding potential in proteins. J Mol Biol 1994;238:777-793.

25 references, page 1 of 2
Abstract
Introduction of Pro residues into helix interiors results in protein destabilization. It is currently unclear if the converse substitution (i.e., replacement of Pro residues that naturally occur in helix interiors would be stabilizing). Maltose-binding protein is a large 370-amino acid protein that contains 21 Pro residues. Of these, three nonconserved residues (P48, P133, and P159) occur at helix interiors. Each of the residues was replaced with Ala and Ser. Stabilities were characterized by differential scanning calorimetry (DSC) as a function of pH and by isothermal urea denaturation studies as a function of temperature. The P48S and P48A mutants were found t...
Subjects
free text keywords: Molecular Biophysics Unit
25 references, page 1 of 2

1. Sauer UH, San DP, Matthews BW. Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions. J Biol Chem 1992;267:2393-2399.

2. Gray TM, Arnoys EJ, Blankespoor S, Born T, Jagar R, Everman R, Plowman D, Stair A, Zhang D. Destabilizing effect of proline substitutions in two helical regions of T4 lysozyme: leucine 66 to proline and leucine 91 to proline. Protein Sci 1996;5:742-751.

3. Gunasekaran K, Nagarajaram HA, Ramakrishnan C, Balaram P. Stereochemical punctuation marks in protein structures: glycine and proline containing helix stop signals. J Mol Biol 1998;275:917-932. [OpenAIRE]

4. Ganesh C, Shah AN, Swaminathan CP, Surolia A, Varadarajan R. Thermodynamic characterization of the reversible, two-state unfolding of maltose binding protein, a large two-domain protein. Biochemistry 1997;36:5020 -5028.

5. Sheshadri S, Lingaraju GM, Varadarajan R. Denaturant mediated unfolding of both native and molten globule states of maltose binding protein are accompanied by large deltaCp's. Protein Sci 1999;8:1689 -1695. [OpenAIRE]

6. Spurlino JC, Lu GY, Quiocho FA. The 2.3-A resolution structure of the maltose-or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. J Biol Chem 1991;266: 5202-5219.

7. Sharff AJ, Rodseth LE, Spurlino JC, Quiocho FA. Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis. Biochemistry 1992;31: 10657-10663.

8. Chakrabarti A, Srivastava S, Swaminathan CP, Surolia A, Varadarajan R. Thermodynamics of replacing an alpha-helical Pro residue in the P40S mutant of Escherichia coli thioredoxin. Protein Sci 1999;8:2455-2459. [OpenAIRE]

9. Duplay P, Bedouelle H, Fowler A, Zabin I, Saurin W, Hofnung M. Sequences of the malE gene and of its product, the maltosebinding protein of Escherichia coli K12. J Biol Chem 1984;259: 10606 -10613.

10. Martineau P, Szmelcman S, Spurlino JC, Quiocho FA, Hofnung M. Genetic approach to the role of tryptophan residues in the activities and fluorescence of a bacterial periplasmic maltosebinding protein. J Mol Biol 1990;214:337-352. [OpenAIRE]

11. Ganesh C, Banerjee A, Shah A, Varadarajan R. Disordered N-terminal residues affect the folding thermodynamics and kinetics of maltose binding protein. FEBS Lett 1999;454:307-311.

12. Schellman JA. The thermodynamic stability of proteins. Annu Rev Biophys Biophys Chem 1987;16:115-137. [OpenAIRE]

13. Chen BL, Schellman JA. Low-temperature unfolding of a mutant of phage T4 lysozyme. I. Equilibrium studies. Biochemistry 1989; 28:685- 691. [OpenAIRE]

14. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE. The Protein Data Bank. Nucleic Acids Res 2000;28:235-242.

15. McDonald IK, Thornton JM. Satisfying hydrogen bonding potential in proteins. J Mol Biol 1994;238:777-793.

25 references, page 1 of 2
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